Week 2: Pepcin, Mucin and Intrinsic Factor Flashcards

1
Q

Where are Chief Cells located?

A

Cryptic pits in the stomach infolds

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2
Q

Chief Cells secrete?

A

Pepsinogen

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3
Q

What is pepsinogen?

A

a precursor to protease which is inactive ‘ogen’ suffix is indicative of inactivity

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4
Q

What types of proteases are there?

A
  • Endoproteases
  • Exoproteases
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5
Q

What is an endoprotease?

A

protease that digests from the middle or not from the ends of proteins

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6
Q

What is an exoprotease?

A

Digests proteins from the terminal ends

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7
Q

what does the suffix ‘ogen’ mean

A

inactive

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8
Q

Why is it important that pepsinogen is inactive?

A

because you don’t want proteases digesting intracellular proteins

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9
Q

What is autoproteolysis?

A

when an inactive protease is able to cleave itself when a certain condition is met (eg pepsinogen to low pH) to create a conformational change which becomes the active protease

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10
Q

What kind of protease is pepsinogen?

A

endoprotease

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11
Q

Optimal pH for pepsinogen?

A

pH of 2-3

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12
Q

What is the active form of pepsinogen?

A

Pepsin

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13
Q

What happens when pepsin exits the stomach into the duodenum?

A

Pepsin activity is reduced or could be 0

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14
Q

what is the typical pH of the duodenum?

A

pH ~8.0

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15
Q

What are goblet cells?

A

filled with translucent material (mucopolysaccharide)

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16
Q

What is the typical structure of a mucopolysaccharide?

A

typically have very short protein domains and very long carbohydrate domains

This structure binds a lot of water by the sugars and interacts with a lot of H-bonds which makes it mucus-like and viscous

17
Q

Why is mucin important?

A

mucin gelatinous layer sits on top of cell surfaces along the lumen of the GI tract

The gelatinous layer protects the cells from active pepsin preventing pepsin from digesting membrane proteins

Goblet cells also secrete HCO3- which is basic

we have low pH in the lumen so the HCO3- binds to the protons to neutralize, however the HCO3- sticks in the mucus which protects the underlying cells from the cells surface preventing disruption of luminal membrane proteins

18
Q

Where does intrinsic factor come from?

A

Parietal cells

19
Q

Intrinsic factor function

A

Vitamin B12

20
Q

Why is vitamin B12 critical?

A
  • Because it is important for 1carbon metabolism
  • maintaining RBCs in an antioxidized state
21
Q

important chemical properties of vitamin B12

A

very hydrophobic so it binds to proteins very tightly

22
Q

How is Vitamin B12 absorbed

A

Vitamin B12 binds to any protein

Pepsin hydrolyzes that protein exposing Vitamin B12 which then binds to intrinsic factor which acts as a carrier

Intrinsic factor+Vitamin B12 is then travels through the intestines to the ileum and there are receptors in the ileum which bind the Intrinsic factor+B12 complex

Intrinisic factor is degraded and releases the B12

B12 enters the blood stream by secretion from the basal surface of the epithelium and complexes with transcobalamin

Transcobalamin is a plasma protein which is specific to bind vitamin B12

The Transcobalamin+B12 complex can then enter cells as needed

23
Q

What is transcobalamin?

A
  • Transcobalamin is a plasma protein which is specific to bind vitamin B12 and acts as a carrier
  • The Transcobalamin+B12 complex can then enter cells as needed